WAG1_ARATH
ID WAG1_ARATH Reviewed; 476 AA.
AC Q9C8M5; O81661;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Serine/threonine-protein kinase WAG1;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase 3;
DE Short=AtPK3;
GN Name=WAG1; Synonyms=PK3; OrderedLocusNames=At1g53700; ORFNames=F22G10.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Ma J., Khanna R., Fukasawa-Akada T., Poisso J., Deitzer G.F., Watson J.C.;
RT "PK3At: an Arabidopsis homolog of the PsPK3 protein kinase from Pisum
RT sativum L.";
RL (er) Plant Gene Register PGR98-172(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16460509; DOI=10.1111/j.1365-313x.2005.02641.x;
RA Santner A.A., Watson J.C.;
RT "The WAG1 and WAG2 protein kinases negatively regulate root waving in
RT Arabidopsis.";
RL Plant J. 45:752-764(2006).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19075219; DOI=10.1073/pnas.0809761106;
RA Cheng Y., Qin G., Dai X., Zhao Y.;
RT "NPY genes and AGC kinases define two key steps in auxin-mediated
RT organogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:21017-21022(2008).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20823065; DOI=10.1242/dev.052456;
RA Dhonukshe P., Huang F., Galvan-Ampudia C.S., Mahonen A.P., Kleine-Vehn J.,
RA Xu J., Quint A., Prasad K., Friml J., Scheres B., Offringa R.;
RT "Plasma membrane-bound AGC3 kinases phosphorylate PIN auxin carriers at
RT TPRXS(N/S) motifs to direct apical PIN recycling.";
RL Development 137:3245-3255(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the regulation of
CC auxin signaling. Acts as a positive regulator of cellular auxin efflux
CC and regulates organ development by enhancing PIN-mediated polar auxin
CC transport. Phosphorylates conserved serine residues in the PIN auxin
CC efflux carriers. Phosphorylation of PIN proteins is required and
CC sufficient for apical-basal PIN polarity that enables directional
CC intercellular auxin fluxes, which mediate differential growth, tissue
CC patterning and organogenesis. Acts as suppressors of root waving.
CC {ECO:0000269|PubMed:16460509, ECO:0000269|PubMed:19075219,
CC ECO:0000269|PubMed:20823065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20823065}.
CC Note=Targeted to the cell periphery.
CC -!- TISSUE SPECIFICITY: Expressed in root tips and lateral root primordia.
CC {ECO:0000269|PubMed:16460509}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis with higher
CC expression in the cotyledon primordia at heart stages.
CC {ECO:0000269|PubMed:19075219}.
CC -!- DISRUPTION PHENOTYPE: Enhanced root waving when grown on agar plates.
CC {ECO:0000269|PubMed:16460509}.
CC -!- MISCELLANEOUS: Over-expression of WAG1 induces a basal-to-apical shift
CC in PIN1, PIN2 and PIN4 localization, resulting in the loss of auxin
CC gradients and strong defects in embryo and seedling roots.
CC {ECO:0000305|PubMed:20823065}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF082391; AAC78477.1; -; Genomic_DNA.
DR EMBL; AC024260; AAG51984.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32983.1; -; Genomic_DNA.
DR EMBL; BT030386; ABO45689.1; -; mRNA.
DR PIR; C96577; C96577.
DR RefSeq; NP_175774.1; NM_104248.4.
DR AlphaFoldDB; Q9C8M5; -.
DR SMR; Q9C8M5; -.
DR IntAct; Q9C8M5; 1.
DR STRING; 3702.AT1G53700.1; -.
DR PaxDb; Q9C8M5; -.
DR PRIDE; Q9C8M5; -.
DR EnsemblPlants; AT1G53700.1; AT1G53700.1; AT1G53700.
DR GeneID; 841807; -.
DR Gramene; AT1G53700.1; AT1G53700.1; AT1G53700.
DR KEGG; ath:AT1G53700; -.
DR Araport; AT1G53700; -.
DR TAIR; locus:2024892; AT1G53700.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9C8M5; -.
DR OMA; GSWNSMG; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q9C8M5; -.
DR PRO; PR:Q9C8M5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8M5; baseline and differential.
DR Genevisible; Q9C8M5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Auxin signaling pathway; Cytoplasm; Developmental protein;
KW Growth regulation; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..476
FT /note="Serine/threonine-protein kinase WAG1"
FT /id="PRO_0000425534"
FT DOMAIN 93..400
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 278
FT /note="Y -> F (in Ref. 1; AAC78477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53820 MW; 743D0B8D46DC0247 CRC64;
MEDDGYYLDT DLDLSFTSTA TDRTFTSSSA RSSLARSSLT LSFNDRLSTA TTPSTTTSSA
ATTLHHRRYD PHWTSIRAAT TLSSDGRLHL RHFKLVRHLG TGNLGRVFLC HLRDCPNPTG
FALKVIDRDV LTAKKISHVE TEAEILSLLD HPFLPTLYAR IDASHYTCLL IDYCPNGDLH
SLLRKQPNNR LPISPVRFFA AEVLVALEYL HALGIVYRDL KPENILIRED GHIMLSDFDL
CFKADVVPTF RSRRFRRTSS SPRKTRRGGG CFSTEVEYER EEIVAEFAAE PVTAFSKSCV
GTHEYLAPEL VAGNGHGSGV DWWAFGIFLY EMLYGTTPFK GGTKEQTLRN IVSNDDVAFT
LEEEGMVEAK DLIEKLLVKD PRKRLGCARG AQDIKRHEFF EGIKWPLIRN YKPPEIRGLV
KKTKAHAGHV TAAVTPRRNK WLWWALSHLL RSKSLSKSSS KIQSNNNYYH YVGKKL
